SpringerProtocols: Abstract: Flavoenzyme Structure and Function: Approaches Using Flavin Analogues

Flavoenzyme Structure and Function: Approaches Using Flavin Analogues

By: Dale Edmondson², Sandro Ghisla²

Abstract

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Flavoenzymes are redox proteins that catalyze a wide diversity of biological reactions ranging from O₂ activation, to aromatic hydroxylations, dehydrogenations, and reactions in which they can accept or donate one or two electrons. In addition, they can fulfill structural and regulatory roles. This diversity is due to the fine tuning of the reactivity of the isoalloxazine ring of the flavin coenzyme by specific interactions with the protein moiety on the particular enzyme it complexes with. Methods to provide specific information on these interactions have relied on three approaches:

1.	Determination of the three-dimensional structure of the flavoenzyme by X-ray diffraction techniques.
2.	Spectroscopic probes of the protein influence on flavin structure by techniques such as nuclear magnetic resonance (NMR), resonance Raman, fluorescence, electron paramagnetic resonance (EPR), and circular dichroism (CD) spectroscopies.
3.	Replacement of the native flavin coenzyme with suitable flavin analogues designed to ask specific questions regarding the reactivity, the accessibility, and the mode of specific interactions with the protein.

Affiliation(s): (2) Departments of Biochemistry and Chemistry, Emory University School of Medicine, Atlanta, GA

Book Title: Flavoprotein Protocols

Series: Methods in Molecular Biology | Volume: 131 | Pub. Date: Jul-01-1999 | Page Range: 157-179 | DOI: 10.1385/1-59259-266-X:157

Subject: Protein Science

References

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